Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches

Lysozyme is often used as a model protein to study interaction with drug molecules and to understand biological processes which help in illuminating the therapeutic effectiveness of the drug. In the present work, in vitro interaction studies of 1-{(2-hydroxyethyl)amino}-2-amino-1,2-dideoxy-<span...

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Autores principales:	Sabiha Parveen, Mohd. Sajid Ali, Hamad A. Al-Lohedan, Sartaj Tabassum
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	lysozyme organotin interaction studies thermodynamics molecular docking Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/f0873eb069e34284b0c15c26df951600
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spelling	oai:doaj.org-article:f0873eb069e34284b0c15c26df9516002021-11-11T18:36:32ZInteraction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches10.3390/molecules262166411420-3049https://doaj.org/article/f0873eb069e34284b0c15c26df9516002021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6641https://doaj.org/toc/1420-3049Lysozyme is often used as a model protein to study interaction with drug molecules and to understand biological processes which help in illuminating the therapeutic effectiveness of the drug. In the present work, in vitro interaction studies of 1-{(2-hydroxyethyl)amino}-2-amino-1,2-dideoxy-<span style="font-variant: small-caps;">d</span>-glucose triphenyl tin (IV) (GATPT) complex with lysozyme were carried out by employing various biophysical methods such as absorption, fluorescence, and circular dichroism (CD) spectroscopies. The experimental results revealed efficient binding affinity of GATPT with lysozyme with intrinsic binding (K<sub>b</sub>) and binding constant (K) values in the order of 10<sup>5</sup> M<sup>−1</sup>. The number of binding sites and thermodynamic parameters ΔG, ΔH, and ΔS at four different temperatures were also calculated and the interaction of GATPT with lysozyme was found to be enthalpy and entropy driven. The CD spectra revealed alterations in the population of α–helical content within the secondary structure of lysozyme in presence of GATPT complex. The morphological analysis of the complex with lysozyme and lysozyme-DNA condensates was carried out by employing confocal and SEM studies. Furthermore, the molecular docking studies confirmed the interaction of GATPT within the larger hydrophobic pocket of the lysozyme via several non-covalent interactions.Sabiha ParveenMohd. Sajid AliHamad A. Al-LohedanSartaj TabassumMDPI AGarticlelysozymeorganotininteraction studiesthermodynamicsmolecular dockingOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6641, p 6641 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	lysozyme organotin interaction studies thermodynamics molecular docking Organic chemistry QD241-441
spellingShingle	lysozyme organotin interaction studies thermodynamics molecular docking Organic chemistry QD241-441 Sabiha Parveen Mohd. Sajid Ali Hamad A. Al-Lohedan Sartaj Tabassum Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
description	Lysozyme is often used as a model protein to study interaction with drug molecules and to understand biological processes which help in illuminating the therapeutic effectiveness of the drug. In the present work, in vitro interaction studies of 1-{(2-hydroxyethyl)amino}-2-amino-1,2-dideoxy-<span style="font-variant: small-caps;">d</span>-glucose triphenyl tin (IV) (GATPT) complex with lysozyme were carried out by employing various biophysical methods such as absorption, fluorescence, and circular dichroism (CD) spectroscopies. The experimental results revealed efficient binding affinity of GATPT with lysozyme with intrinsic binding (K<sub>b</sub>) and binding constant (K) values in the order of 10<sup>5</sup> M<sup>−1</sup>. The number of binding sites and thermodynamic parameters ΔG, ΔH, and ΔS at four different temperatures were also calculated and the interaction of GATPT with lysozyme was found to be enthalpy and entropy driven. The CD spectra revealed alterations in the population of α–helical content within the secondary structure of lysozyme in presence of GATPT complex. The morphological analysis of the complex with lysozyme and lysozyme-DNA condensates was carried out by employing confocal and SEM studies. Furthermore, the molecular docking studies confirmed the interaction of GATPT within the larger hydrophobic pocket of the lysozyme via several non-covalent interactions.
format	article
author	Sabiha Parveen Mohd. Sajid Ali Hamad A. Al-Lohedan Sartaj Tabassum
author_facet	Sabiha Parveen Mohd. Sajid Ali Hamad A. Al-Lohedan Sartaj Tabassum
author_sort	Sabiha Parveen
title	Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
title_short	Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
title_full	Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
title_fullStr	Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
title_full_unstemmed	Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches
title_sort	interaction of carrier protein with potential metallic drug candidate <i>n</i>-glycoside ‘gatpt’: validation by multi-spectroscopic and molecular docking approaches
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f0873eb069e34284b0c15c26df951600
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Interaction of Carrier Protein with Potential Metallic Drug Candidate <i>N</i>-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches

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